The sucker ring teeth (SRT) of Humboldt squid exhibit mechanical properties that rival those of robust engineered synthetic polymers. Remarkably, these properties 'are' achieved without a mineral phase or covalent cross-links. Instead, SRT are exclusively made of silk-like proteins called 'suckerins"; which assemble into nanoconfined β-sheet reinforced supramolecular networks. In this study, three streamlined strategies for full-length recombinant suckerin protein production and purification were developed. Recombinant suckerin exhibited high solubility and colloidal stability in aqueous-based solvents. In addition, the colloidal suspensions exhibited a concentration-dependent conformational switch, from random coil to, β-sheet enriched structures. Our results demonstrate that recombinant suckerin can be produced in a facile mahrier-jn E, coli-and processed from mild aqueous solutions into materials enriched in β-sheets. We suggest that recombinant -suckein-based materials offer potential for a range of biomedical and engineering applications.
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